SERC_STRMK
ID SERC_STRMK Reviewed; 361 AA.
AC B2FKF0;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Phosphoserine aminotransferase {ECO:0000255|HAMAP-Rule:MF_00160};
DE EC=2.6.1.52 {ECO:0000255|HAMAP-Rule:MF_00160};
DE AltName: Full=Phosphohydroxythreonine aminotransferase {ECO:0000255|HAMAP-Rule:MF_00160};
DE Short=PSAT {ECO:0000255|HAMAP-Rule:MF_00160};
GN Name=serC {ECO:0000255|HAMAP-Rule:MF_00160}; OrderedLocusNames=Smlt3098;
OS Stenotrophomonas maltophilia (strain K279a).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX NCBI_TaxID=522373;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K279a;
RX PubMed=18419807; DOI=10.1186/gb-2008-9-4-r74;
RA Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A.,
RA Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E.,
RA Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S.,
RA Quail M.A., Rajandream M.A., Harris D., Churcher C., Bentley S.D.,
RA Parkhill J., Thomson N.R., Avison M.B.;
RT "The complete genome, comparative and functional analysis of
RT Stenotrophomonas maltophilia reveals an organism heavily shielded by drug
RT resistance determinants.";
RL Genome Biol. 9:R74.1-R74.13(2008).
CC -!- FUNCTION: Catalyzes the reversible conversion of 3-
CC phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-
CC phosphonooxybutanoate to phosphohydroxythreonine. {ECO:0000255|HAMAP-
CC Rule:MF_00160}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + O-phospho-L-serine = 3-phosphooxypyruvate +
CC L-glutamate; Xref=Rhea:RHEA:14329, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:18110, ChEBI:CHEBI:29985, ChEBI:CHEBI:57524; EC=2.6.1.52;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00160};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + 4-(phosphooxy)-L-threonine = (R)-3-hydroxy-2-
CC oxo-4-phosphooxybutanoate + L-glutamate; Xref=Rhea:RHEA:16573,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:58452,
CC ChEBI:CHEBI:58538; EC=2.6.1.52; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00160};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00160};
CC Note=Binds 1 pyridoxal phosphate per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00160};
CC -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC 3-phospho-D-glycerate: step 2/3. {ECO:0000255|HAMAP-Rule:MF_00160}.
CC -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis;
CC pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 3/5.
CC {ECO:0000255|HAMAP-Rule:MF_00160}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00160}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00160}.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. SerC subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_00160}.
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DR EMBL; AM743169; CAQ46546.1; -; Genomic_DNA.
DR RefSeq; WP_012480720.1; NC_010943.1.
DR PDB; 6XDK; X-ray; 1.60 A; A/B/C/D=1-361.
DR PDBsum; 6XDK; -.
DR AlphaFoldDB; B2FKF0; -.
DR SMR; B2FKF0; -.
DR STRING; 522373.Smlt3098; -.
DR EnsemblBacteria; CAQ46546; CAQ46546; Smlt3098.
DR KEGG; sml:Smlt3098; -.
DR PATRIC; fig|522373.3.peg.2901; -.
DR eggNOG; COG1932; Bacteria.
DR HOGENOM; CLU_034866_0_2_6; -.
DR OMA; GYRASMY; -.
DR OrthoDB; 996960at2; -.
DR UniPathway; UPA00135; UER00197.
DR UniPathway; UPA00244; UER00311.
DR Proteomes; UP000008840; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004648; F:O-phospho-L-serine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_00160; SerC_aminotrans_5; 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR InterPro; IPR022278; Pser_aminoTfrase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43247; PTHR43247; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF000525; SerC; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR01364; serC_1; 1.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aminotransferase; Cytoplasm;
KW Pyridoxal phosphate; Pyridoxine biosynthesis; Reference proteome;
KW Serine biosynthesis; Transferase.
FT CHAIN 1..361
FT /note="Phosphoserine aminotransferase"
FT /id="PRO_1000097222"
FT BINDING 42
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160"
FT BINDING 76..77
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160"
FT BINDING 102
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160"
FT BINDING 152
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160"
FT BINDING 172
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160"
FT BINDING 195
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160"
FT BINDING 237..238
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160"
FT MOD_RES 196
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:6XDK"
FT HELIX 16..25
FT /evidence="ECO:0007829|PDB:6XDK"
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:6XDK"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:6XDK"
FT HELIX 44..61
FT /evidence="ECO:0007829|PDB:6XDK"
FT STRAND 67..74
FT /evidence="ECO:0007829|PDB:6XDK"
FT HELIX 75..87
FT /evidence="ECO:0007829|PDB:6XDK"
FT STRAND 93..100
FT /evidence="ECO:0007829|PDB:6XDK"
FT HELIX 101..110
FT /evidence="ECO:0007829|PDB:6XDK"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:6XDK"
FT STRAND 114..121
FT /evidence="ECO:0007829|PDB:6XDK"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:6XDK"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:6XDK"
FT STRAND 145..151
FT /evidence="ECO:0007829|PDB:6XDK"
FT TURN 152..155
FT /evidence="ECO:0007829|PDB:6XDK"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:6XDK"
FT TURN 174..178
FT /evidence="ECO:0007829|PDB:6XDK"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:6XDK"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:6XDK"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:6XDK"
FT STRAND 204..209
FT /evidence="ECO:0007829|PDB:6XDK"
FT HELIX 210..214
FT /evidence="ECO:0007829|PDB:6XDK"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:6XDK"
FT HELIX 226..231
FT /evidence="ECO:0007829|PDB:6XDK"
FT TURN 232..234
FT /evidence="ECO:0007829|PDB:6XDK"
FT HELIX 241..256
FT /evidence="ECO:0007829|PDB:6XDK"
FT HELIX 259..279
FT /evidence="ECO:0007829|PDB:6XDK"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:6XDK"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:6XDK"
FT STRAND 296..302
FT /evidence="ECO:0007829|PDB:6XDK"
FT HELIX 306..318
FT /evidence="ECO:0007829|PDB:6XDK"
FT TURN 328..330
FT /evidence="ECO:0007829|PDB:6XDK"
FT STRAND 332..336
FT /evidence="ECO:0007829|PDB:6XDK"
FT HELIX 343..360
FT /evidence="ECO:0007829|PDB:6XDK"
SQ SEQUENCE 361 AA; 39037 MW; 97C627265CD27603 CRC64;
MTRAFNFSAG PATLPESVLR QAQAEMLDWH GSGASIVEMS HRGAEFMSVA AEAEADLRRL
LDIPDDYAVL FLSGGATTQQ ALIPLNFAAP GQRADYVVSG HWGKTAVKQA GVYVDVNIAA
SSEANGYREL PARADWQLSR DAAYVHITAN ETIHGVEFRD VPDTGNVPLI ADFSSSIASE
PLDVRRYGVI YAGAQKNLGP VGVAVMIIRR DLLERSGQPR ADIFDYRSHV ARDSMLNTPP
TWNWYLAGLV FKWMLAEGGV TEFAKRNAAK AALVYGAIDG SGGFYRNEVA YAARSRMNIP
FFLPDAELDA RFVAEAKAAG LLALKGHKVV GGIRASLYNA MPLAGAEALV AFMADFQQRH
G
